The protein contains paramagnetic copper(II), whose electronic relaxation times are quite unfavorable for NMR solution studies. The structure has been solved on the basis of 1041 meaningful NOESY cross peaks, 18 1D NOEs, 26 T1 values, 96 dihedral angle constraints and 18 H-bonds. The detection of broad hyperfine shifted signals and their full assignment allowed the identification of the copper(II) ligands and the determination of the Cu-S-C-H dihedral angle for the coordinated cysteine. The global root mean square deviation from the mean structure for the solution structure family is 0.72 and 1.16 for backbone and heavy atoms, respectively.